{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,19]],"date-time":"2026-09-19T20:39:46Z","timestamp":1789850386075,"version":"4.0.1"},"reference-count":68,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2014,4,14]],"date-time":"2014-04-14T00:00:00Z","timestamp":1397433600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecular Microbiology"],"published-print":{"date-parts":[[2014,5]]},"abstract":"Summary<\/jats:title>In this study we uncover two genes in L<\/jats:italic><\/jats:styled-content>actobacillus brevis<\/jats:italic>\u2005ATCC<\/jats:styled-content> 367, tstT<\/jats:italic><\/jats:styled-content> and tstR<\/jats:italic><\/jats:styled-content>, encoding for a rhodanese and a transcriptional regulator involved in cyanide detoxification. TstT<\/jats:styled-content> (LVIS<\/jats:styled-content>_0852) belongs to a new class of thiosulphate:cyanide sulphurtransferases. We found that TstR<\/jats:styled-content> (LVIS<\/jats:styled-content>_0853) modulates both the expression and the activity of the downstream\u2010encoded tstT<\/jats:italic><\/jats:styled-content>. The TstR<\/jats:styled-content> binding site was identified at \u22121 to +33, from tstR<\/jats:italic><\/jats:styled-content> transcriptional start site. EMSA<\/jats:styled-content> revealed that sulphite, a product of the reaction catalysed by TstT<\/jats:styled-content>, improved the interaction between TstR<\/jats:styled-content>:PtstR<\/jats:sub><\/jats:italic><\/jats:styled-content>, while F<\/jats:styled-content>e(III<\/jats:styled-content>) disrupted this interaction. Site\u2010directed mutagenesis in TstR<\/jats:styled-content> identified M<\/jats:styled-content>64 as a key residue in sulphite recognition, while residues H<\/jats:styled-content>136\u2010H<\/jats:styled-content>139\u2010C<\/jats:styled-content>167\u2010M<\/jats:styled-content>171 formed a pocket for ferric iron co\u2010ordination. In addition to its role as a transcriptional repressor, TstR<\/jats:styled-content> is also involved in regulating the thiosulphate:cyanide sulphurtransferase activity of TstT<\/jats:styled-content>. A threefold increase in TstT<\/jats:styled-content> activity was observed in the presence of TstR<\/jats:styled-content>, which was enhanced by the addition of F<\/jats:styled-content>e(III<\/jats:styled-content>). Overexpression of the tstRT<\/jats:italic><\/jats:styled-content> operon was found to increase the cyanide tolerance of L<\/jats:italic><\/jats:styled-content>.\u2009brevis<\/jats:italic> and E<\/jats:italic><\/jats:styled-content>scherichia coli<\/jats:italic>. The protein\u2013protein interaction between TstR<\/jats:styled-content> and TstT<\/jats:styled-content> described herein represents a novel mechanism for regulation of enzymatic activity by a transcriptional regulator.<\/jats:p>","DOI":"10.1111\/mmi.12598","type":"journal-article","created":{"date-parts":[[2014,3,31]],"date-time":"2014-03-31T10:23:26Z","timestamp":1396261406000},"page":"853-871","source":"Crossref","is-referenced-by-count":6,"title":["A dual role of the transcriptional regulator TstR<\/scp> provides insights into cyanide detoxification in L<\/i><\/scp>actobacillus brevis<\/i>"],"prefix":"10.1111","volume":"92","author":[{"given":"Fernando A.","family":"Pagliai","sequence":"first","affiliation":[{"name":"Department of Microbiology and Cell Science Genetics Institute Institute of Food and Agricultural Sciences University of Florida 2033 Mowry road. 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